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Protein

Aryl hydrocarbon receptor nuclear translocator-like protein 1

Gene

ARNTL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. ARNTL/BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function; regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway; regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes; rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART and KLF11. The CLOCK-ARNTL/BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The NPAS2-ARNTL/BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. The preferred binding motif for the CLOCK-ARNTL/BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking Ala residue in addition to the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while ARNTL binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-ARNTL/BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). Essential for the rhythmic interaction of CLOCK with ASS1 and plays a critical role in positively regulating CLOCK-mediated acetylation of ASS1 (PubMed:28985504).7 Publications

Miscellaneous

CLOCK-ARNTL/BMAL1 double mutations within the PAS domains result in synergistic desensitization to high levels of CRY on repression of CLOCK-ARNTL/BMAL1 transcriptional activity of PER1 and, disrupt circadian rhythmicity.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

There is conflicting data about the effect of NAD cofactors on activity. PubMed:11441146 suggests that the redox state of the cell can modulate the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer; NADH and NADPH enhance the DNA-binding activity of the heterodimer. PubMed:23229515 reports that NADH and NADPH have no significant effect on DNA-binding activity of the CLOCK-ARNTL/BMAL1 heterodimer.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei125Important for interaction with CLOCK1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding
Biological processBiological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1368108 BMAL1:CLOCK,NPAS2 activates circadian gene expression
R-HSA-1989781 PPARA activates gene expression
R-HSA-400253 Circadian Clock

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O00327

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Aryl hydrocarbon receptor nuclear translocator-like protein 1
Alternative name(s):
Basic-helix-loop-helix-PAS protein MOP3
Brain and muscle ARNT-like 1
Class E basic helix-loop-helix protein 5
Short name:
bHLHe5
Member of PAS protein 3
PAS domain-containing protein 3
bHLH-PAS protein JAP3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ARNTL
Synonyms:BHLHE5, BMAL1, MOP3, PASD3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000133794.17

Human Gene Nomenclature Database

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HGNCi
HGNC:701 ARNTL

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602550 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O00327

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi9S → A or E: Enhanced PER1 reporter activity by CLOCK-ARNTL/BMAL1. 1 Publication1
Mutagenesisi9S → F: 2-2.5-fold increase in CLOCK-BMAL1 transcriptional activity in the absence of CRY1. No change in repression activity in the presence of CRY1. 1 Publication1
Mutagenesisi10S → A or E: Enhanced PER1 reporter activity by CLOCK-ARNTL/BMAL1. 1 Publication1
Mutagenesisi10S → L: 2-2.5-fold increase in CLOCK-ARNTL/BMAL1 transcriptional activity in the absence of CRY1. No change in repression activity in the presence of CRY1. 1 Publication1
Mutagenesisi78S → E: Phosphomimetic mutant which severely impairs DNA binding and CLOCK-ARNTL/BMAL1 transcriptional activity. 1 Publication1
Mutagenesisi88M → F: No effect on CLOCK binding. 1 Publication1
Mutagenesisi90S → E: Phosphomimetic mutant with no effect on DNA binding or CLOCK-ARNTL/BMAL1 transcriptional activity. 1 Publication1
Mutagenesisi125L → H: Impaired CLOCK binding. 1 Publication1
Mutagenesisi611A → S or T: Increased desensitization to CRY1, in the presence of CLOCK. Approximately 2-fold increase in CLOCK-ARNTL/BMAL1 transcriptional activity in the absence of CRY1; when associated with E-407. 1 Publication1
Mutagenesisi612G → E: Increased desensitization to CRY1, in the presence of CLOCK. Approximately 2-fold increase in CLOCK-ARNTL/BMAL1 transcriptional activity in the absence of CRY1. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
406

Open Targets

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OpenTargetsi
ENSG00000133794

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24996

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ARNTL

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001271561 – 626Aryl hydrocarbon receptor nuclear translocator-like protein 1Add BLAST626

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei17Phosphoserine; by GSK3-betaBy similarity1
Modified residuei21Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei78Phosphoserine1 Publication1
Modified residuei90Phosphoserine; by CK2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki252Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)By similarity
Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei538N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated, leading to its proteasomal degradation (PubMed:24728990). Deubiquitinated by USP9X (PubMed:29626158).2 Publications
O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-ARNTL/BMAL1 heterodimer thereby increasing CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2/3 and CRY1/2.By similarity
Acetylated on Lys-538 upon dimerization with CLOCK. Acetylation facilitates CRY1-mediated repression. Deacetylated by SIRT1, which may result in decreased protein stability.By similarity
Phosphorylated upon dimerization with CLOCK. Phosphorylation enhances the transcriptional activity, alters the subcellular localization and decreases the stability of the CLOCK-ARNTL/BMAL1 heterodimer by promoting its degradation. Phosphorylation shows circadian variations in the liver with a peak between CT10 to CT14. Phosphorylation at Ser-90 by CK2 is essential for its nuclear localization, its interaction with CLOCK and controls CLOCK nuclear entry (By similarity). Dephosphorylation at Ser-78 is important for dimerization with CLOCK and transcriptional activity (PubMed:23229515).By similarity1 Publication
Sumoylated on Lys-259 upon dimerization with CLOCK. Predominantly conjugated to poly-SUMO2/3 rather than SUMO1 and the level of these conjugates undergo rhythmic variation, peaking at CT9-CT12. Sumoylation localizes it exclusively to the PML body and promotes its ubiquitination in the PML body, ubiquitin-dependent proteasomal degradation and the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer.By similarity
Undergoes lysosome-mediated degradation in a time-dependent manner in the liver.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O00327

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O00327

PeptideAtlas

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PeptideAtlasi
O00327

PRoteomics IDEntifications database

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PRIDEi
O00327

ProteomicsDB human proteome resource

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ProteomicsDBi
47841
47842 [O00327-1]
47843 [O00327-3]
47844 [O00327-4]
47845 [O00327-5]
47846 [O00327-6]
47847 [O00327-7]
47848 [O00327-8]
47849 [O00327-9]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O00327

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
O00327

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Hair follicles (at protein level). Highly expressed in the adult brain, skeletal muscle and heart.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000133794 Expressed in 217 organ(s), highest expression level in left lobe of thyroid gland

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O00327 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O00327 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB045962
HPA050938

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the circadian clock oscillator which includes the CRY1/2 proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER1/2/3 proteins (By similarity). Forms a heterodimer with CLOCK (PubMed:9616112, PubMed:23229515). The CLOCK-ARNTL/BMAL1 heterodimer is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and, for phosphorylation of both CLOCK and ARNTL/BMAL1 (By similarity). Part of a nuclear complex which also includes RACK1 and PRKCA; RACK1 and PRKCA are recruited to the complex in a circadian manner (By similarity). Interacts with NPAS2 (By similarity). Interacts with EZH2 (By similarity). Interacts with SUMO3 (By similarity). Interacts with SIRT1 (By similarity). Interacts with AHR (PubMed:9079689). Interacts with ID1, ID2 and ID3 (By similarity). Interacts with DDX4 (By similarity). Interacts with OGT (By similarity). Interacts with EED and SUZ12 (By similarity). Interacts with MTA1 (By similarity). Interacts with CIART (PubMed:24385426). Interacts with HSP90 (PubMed:9079689). Interacts with KAT2B and EP300 (PubMed:14645221). Interacts with BHLHE40/DEC1 and BHLHE41/DEC2 (By similarity). Interacts with RELB and the interaction is enhanced in the presence of CLOCK (By similarity). Interacts with PER1, PER2, CRY1 and CRY2 and this interaction requires a translocation to the nucleus (By similarity). Interaction of the CLOCK-ARNTL/BMAL1 heterodimer with PER or CRY inhibits transcription activation (By similarity). Interaction of the CLOCK-ARNTL/BMAL1 with CRY1 is independent of DNA but with PER2 is off DNA (By similarity). The CLOCK-ARNTL/BMAL1 heterodimer interacts with GSK3B (By similarity). Interacts with KDM5A (PubMed:21960634). Interacts with KMT2A; in a circadian manner (By similarity). Interacts with UBE3A (PubMed:24728990). Interacts with PRKCG (By similarity). Interacts with MAGEL2 (By similarity). Interacts with NCOA2 (By similarity). Interacts with THRAP3 (By similarity). The CLOCK-ARNTL/BMAL1 heterodimer interacts with PASD1 (PubMed:25936801). Interacts with PASD1 (PubMed:25936801). Interacts with USP9X (PubMed:29626158).By similarity10 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei77Interaction with E-box DNA1 Publication1
Sitei80Interaction with E-box DNA1 Publication1
Sitei81Interaction with E-box DNA1 Publication1
Sitei85Interaction with E-box DNA1 Publication1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106899, 61 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3229 CLOCK-BMAL1 transcription complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O00327

Database of interacting proteins

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DIPi
DIP-46008N

Protein interaction database and analysis system

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IntActi
O00327, 13 interactors

Molecular INTeraction database

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MINTi
O00327

STRING: functional protein association networks

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STRINGi
9606.ENSP00000374357

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1626
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4H10X-ray2.40A66-128[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O00327

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O00327

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini72 – 125bHLHPROSITE-ProRule annotationAdd BLAST54
Domaini143 – 215PAS 1PROSITE-ProRule annotationAdd BLAST73
Domaini326 – 396PAS 2PROSITE-ProRule annotationAdd BLAST71
Domaini401 – 444PACAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni508 – 588Interaction with CIARTBy similarityAdd BLAST81

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi36 – 41Nuclear localization signalBy similarity6
Motifi142 – 152Nuclear export signal 1By similarityAdd BLAST11
Motifi361 – 369Nuclear export signal 2By similarity9

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3561 Eukaryota
ENOG410XRJI LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157523

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234379

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG107503

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O00327

KEGG Orthology (KO)

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KOi
K02296

Identification of Orthologs from Complete Genome Data

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OMAi
EKINTNC

Database of Orthologous Groups

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OrthoDBi
331262at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O00327

TreeFam database of animal gene trees

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TreeFami
TF319983

Family and domain databases

Conserved Domains Database

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CDDi
cd00083 HLH, 1 hit
cd00130 PAS, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.280.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
IPR001067 Nuc_translocat
IPR001610 PAC
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold

Pfam protein domain database

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Pfami
View protein in Pfam
PF00010 HLH, 1 hit
PF00989 PAS, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00785 NCTRNSLOCATR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00353 HLH, 1 hit
SM00086 PAC, 1 hit
SM00091 PAS, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00229 sensory_box, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50888 BHLH, 1 hit
PS50112 PAS, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (9+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 9 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 9 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

Isoform BMAL1B (identifier: O00327-2) [UniParc]FASTAAdd to basket
Also known as: JAP3

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSSTDYQESM
60 70 80 90 100
DTDKDDPHGR LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP
110 120 130 140 150
TCNAMSRKLD KLTVLRMAVQ HMKTLRGATN PYTEANYKPT FLSDDELKHL
160 170 180 190 200
ILRAADGFLF VVGCDRGKIL FVSESVFKIL NYSQNDLIGQ SLFDYLHPKD
210 220 230 240 250
IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC SGARRSFFCR
260 270 280 290 300
MKCNRPSVKV EDKDFPSTCS KKKADRKSFC TIHSTGYLKS WPPTKMGLDE
310 320 330 340 350
DNEPDNEGCN LSCLVAIGRL HSHVVPQPVN GEIRVKSMEY VSRHAIDGKF
360 370 380 390 400
VFVDQRATAI LAYLPQELLG TSCYEYFHQD DIGHLAECHR QVLQTREKIT
410 420 430 440 450
TNCYKFKIKD GSFITLRSRW FSFMNPWTKE VEYIVSTNTV VLANVLEGGD
460 470 480 490 500
PTFPQLTASP HSMDSMLPSG EGGPKRTHPT VPGIPGGTRA GAGKIGRMIA
510 520 530 540 550
EEIMEIHRIR GSSPSSCGSS PLNITSTPPP DASSPGGKKI LNGGTPDIPS
560 570 580 590 600
SGLLSGQAQE NPGYPYSDSS SILGENPHIG IDMIDNDQGS SSPSNDEAAM
610 620
AVIMSLLEAD AGLGGPVDFS DLPWPL
Length:626
Mass (Da):68,762
Last modified:August 15, 2003 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i820F0E07DC6265A6
GO
Isoform BMAL1A (identifier: O00327-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKGSSTDYQ → MINI

Show »
Length:583
Mass (Da):64,207
Checksum:i2AA8E7EEB4A71119
GO
Isoform BMAL1C (identifier: O00327-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     224-224: T → R
     225-626: Missing.

Show »
Length:224
Mass (Da):25,353
Checksum:i0A0580AEDC5A45A0
GO
Isoform BMAL1D (identifier: O00327-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-391: Missing.

Show »
Length:508
Mass (Da):55,462
Checksum:i5FAB2403FD8AAB32
GO
Isoform BMAL1E (identifier: O00327-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-301: SFCTIHSTGYLKSWPPTKMGLDED → AFCTIHSTGYFGIFTTRTSRHIVL
     302-626: Missing.

Show »
Length:301
Mass (Da):33,922
Checksum:iEC942D8A9C9219B3
GO
Isoform BMAL1F (identifier: O00327-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     443-526: ANVLEGGDPT...CGSSPLNITS → SRVDTGHLGQ...QGEPGLGQEK
     527-626: Missing.

Show »
Length:526
Mass (Da):59,242
Checksum:iED01AF63A26CE4E0
GO
Isoform MOP3 (identifier: O00327-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MADQRMDISS...MDTDKDDPHG → MSKEAVSLWA...CFYLLLFPPP

Show »
Length:624
Mass (Da):68,828
Checksum:i7A3FD8FAE5E496D7
GO
Isoform 8 (identifier: O00327-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-274: Missing.

Show »
Length:625
Mass (Da):68,691
Checksum:i3F3F7D5688A6FFE2
GO
Isoform 9 (identifier: O00327-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKGSSTDYQ → MINI
     274-274: Missing.

Show »
Length:582
Mass (Da):64,136
Checksum:iE8D6943E4DD24037
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PPV4E9PPV4_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
141Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PKF0E9PKF0_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
135Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PI92E9PI92_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
72Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PL54E9PL54_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
100Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PRB1E9PRB1_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
46Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YER9H0YER9_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
171Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PKN1E9PKN1_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
59Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PKG7E9PKG7_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
76Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PSD2E9PSD2_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
23Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PNI4E9PNI4_HUMAN
Aryl hydrocarbon receptor nuclear t...
ARNTL
60Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti69R → G in AAC51213 (PubMed:9079689).Curated1
Sequence conflicti123K → R in BAA19935 (PubMed:9144434).Curated1
Sequence conflicti173S → P in BAA19939 (PubMed:9144434).Curated1
Sequence conflicti259K → N in BAA19938 (PubMed:9144434).Curated1
Sequence conflicti264D → N in BAA19938 (PubMed:9144434).Curated1
Sequence conflicti418S → N in BAA19937 (PubMed:9144434).Curated1
Sequence conflicti513 – 514SP → LR in AAC51213 (PubMed:9079689).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0020951 – 59MADQR…DDPHG → MSKEAVSLWALTVSLQPPVP LCVCREMTGSGRRKQQCVTL PFISRELCFYLLLFPPP in isoform MOP3. 1 PublicationAdd BLAST59
Alternative sequenceiVSP_0020941 – 47MADQR…STDYQ → MINI in isoform BMAL1A and isoform 9. 2 PublicationsAdd BLAST47
Alternative sequenceiVSP_002096224T → R in isoform BMAL1C. Curated1
Alternative sequenceiVSP_002097225 – 626Missing in isoform BMAL1C. CuratedAdd BLAST402
Alternative sequenceiVSP_002098274 – 391Missing in isoform BMAL1D. CuratedAdd BLAST118
Alternative sequenceiVSP_035457274Missing in isoform 8 and isoform 9. 2 Publications1
Alternative sequenceiVSP_002099278 – 301SFCTI…GLDED → AFCTIHSTGYFGIFTTRTSR HIVL in isoform BMAL1E. CuratedAdd BLAST24
Alternative sequenceiVSP_002100302 – 626Missing in isoform BMAL1E. CuratedAdd BLAST325
Alternative sequenceiVSP_002101443 – 526ANVLE…LNITS → SRVDTGHLGQVERCTVLSRP NSRFLIAGMFTEPTSWKAGT QPSHSSQHPPTAWTACCPLE KVAQRGPTPLFQGFQGEPGL GQEK in isoform BMAL1F. CuratedAdd BLAST84
Alternative sequenceiVSP_002102527 – 626Missing in isoform BMAL1F. CuratedAdd BLAST100

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D89722 mRNA Translation: BAA19968.1
AB000812 mRNA Translation: BAA19935.1
AB000813 Genomic DNA Translation: BAA19936.1
AB000814 mRNA Translation: BAA19937.1
AB000815 mRNA Translation: BAA19938.1
AB000816 mRNA Translation: BAA19939.1
U51627 mRNA Translation: AAC51213.1
U60415 mRNA Translation: AAB37248.1
AF044288 mRNA Translation: AAC24353.1
AK095749 mRNA Translation: BAG53120.1
AK291510 mRNA Translation: BAF84199.1
EF015894 Genomic DNA Translation: ABM64205.1
AC016884 Genomic DNA No translation available.
AC022878 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW68504.1
CH471064 Genomic DNA Translation: EAW68505.1
CH471064 Genomic DNA Translation: EAW68510.1
CH471064 Genomic DNA Translation: EAW68511.1
CH471064 Genomic DNA Translation: EAW68513.1
BC016674 mRNA Translation: AAH16674.1
BC031214 mRNA Translation: AAH31214.1
BC041129 mRNA Translation: AAH41129.2

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31430.1 [O00327-8]
CCDS44543.1 [O00327-9]
CCDS73259.1 [O00327-2]
CCDS76387.1 [O00327-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC5405
JC5407
PC4288
PC4289

NCBI Reference Sequences

More...
RefSeqi
NP_001025443.1, NM_001030272.2 [O00327-8]
NP_001025444.1, NM_001030273.2 [O00327-9]
NP_001169.3, NM_001178.5 [O00327-8]
NP_001284648.1, NM_001297719.1 [O00327-2]
NP_001284651.1, NM_001297722.1 [O00327-2]
NP_001284653.1, NM_001297724.1 [O00327-1]
XP_011518414.1, XM_011520112.2
XP_011518415.1, XM_011520113.1
XP_016873231.1, XM_017017742.1
XP_016873232.1, XM_017017743.1
XP_016873235.1, XM_017017746.1
XP_016873236.1, XM_017017747.1
XP_016873237.1, XM_017017748.1 [O00327-9]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.65734

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000389707; ENSP00000374357; ENSG00000133794 [O00327-8]
ENST00000401424; ENSP00000385915; ENSG00000133794 [O00327-1]
ENST00000403290; ENSP00000384517; ENSG00000133794 [O00327-2]
ENST00000403482; ENSP00000385897; ENSG00000133794 [O00327-7]
ENST00000403510; ENSP00000385581; ENSG00000133794 [O00327-9]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
406

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:406

UCSC genome browser

More...
UCSCi
uc001mko.4 human [O00327-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89722 mRNA Translation: BAA19968.1
AB000812 mRNA Translation: BAA19935.1
AB000813 Genomic DNA Translation: BAA19936.1
AB000814 mRNA Translation: BAA19937.1
AB000815 mRNA Translation: BAA19938.1
AB000816 mRNA Translation: BAA19939.1
U51627 mRNA Translation: AAC51213.1
U60415 mRNA Translation: AAB37248.1
AF044288 mRNA Translation: AAC24353.1
AK095749 mRNA Translation: BAG53120.1
AK291510 mRNA Translation: BAF84199.1
EF015894 Genomic DNA Translation: ABM64205.1
AC016884 Genomic DNA No translation available.
AC022878 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW68504.1
CH471064 Genomic DNA Translation: EAW68505.1
CH471064 Genomic DNA Translation: EAW68510.1
CH471064 Genomic DNA Translation: EAW68511.1
CH471064 Genomic DNA Translation: EAW68513.1
BC016674 mRNA Translation: AAH16674.1
BC031214 mRNA Translation: AAH31214.1
BC041129 mRNA Translation: AAH41129.2
CCDSiCCDS31430.1 [O00327-8]
CCDS44543.1 [O00327-9]
CCDS73259.1 [O00327-2]
CCDS76387.1 [O00327-1]
PIRiJC5405
JC5407
PC4288
PC4289
RefSeqiNP_001025443.1, NM_001030272.2 [O00327-8]
NP_001025444.1, NM_001030273.2 [O00327-9]
NP_001169.3, NM_001178.5 [O00327-8]
NP_001284648.1, NM_001297719.1 [O00327-2]
NP_001284651.1, NM_001297722.1 [O00327-2]
NP_001284653.1, NM_001297724.1 [O00327-1]
XP_011518414.1, XM_011520112.2
XP_011518415.1, XM_011520113.1
XP_016873231.1, XM_017017742.1
XP_016873232.1, XM_017017743.1
XP_016873235.1, XM_017017746.1
XP_016873236.1, XM_017017747.1
XP_016873237.1, XM_017017748.1 [O00327-9]
UniGeneiHs.65734

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4H10X-ray2.40A66-128[»]
ProteinModelPortaliO00327
SMRiO00327
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106899, 61 interactors
ComplexPortaliCPX-3229 CLOCK-BMAL1 transcription complex
CORUMiO00327
DIPiDIP-46008N
IntActiO00327, 13 interactors
MINTiO00327
STRINGi9606.ENSP00000374357

PTM databases

iPTMnetiO00327
PhosphoSitePlusiO00327

Polymorphism and mutation databases

BioMutaiARNTL

Proteomic databases

jPOSTiO00327
PaxDbiO00327
PeptideAtlasiO00327
PRIDEiO00327
ProteomicsDBi47841
47842 [O00327-1]
47843 [O00327-3]
47844 [O00327-4]
47845 [O00327-5]
47846 [O00327-6]
47847 [O00327-7]
47848 [O00327-8]
47849 [O00327-9]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
406
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389707; ENSP00000374357; ENSG00000133794 [O00327-8]
ENST00000401424; ENSP00000385915; ENSG00000133794 [O00327-1]
ENST00000403290; ENSP00000384517; ENSG00000133794 [O00327-2]
ENST00000403482; ENSP00000385897; ENSG00000133794 [O00327-7]
ENST00000403510; ENSP00000385581; ENSG00000133794 [O00327-9]
GeneIDi406
KEGGihsa:406
UCSCiuc001mko.4 human [O00327-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
406
DisGeNETi406
EuPathDBiHostDB:ENSG00000133794.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ARNTL
HGNCiHGNC:701 ARNTL
HPAiCAB045962
HPA050938
MIMi602550 gene
neXtProtiNX_O00327
OpenTargetsiENSG00000133794
PharmGKBiPA24996

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3561 Eukaryota
ENOG410XRJI LUCA
GeneTreeiENSGT00940000157523
HOGENOMiHOG000234379
HOVERGENiHBG107503
InParanoidiO00327
KOiK02296
OMAiEKINTNC
OrthoDBi331262at2759
PhylomeDBiO00327
TreeFamiTF319983

Enzyme and pathway databases

ReactomeiR-HSA-1368108 BMAL1:CLOCK,NPAS2 activates circadian gene expression
R-HSA-1989781 PPARA activates gene expression
R-HSA-400253 Circadian Clock
SIGNORiO00327

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ARNTL human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ARNTL

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
406

Protein Ontology

More...
PROi
PR:O00327

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
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Gene expression databases

BgeeiENSG00000133794 Expressed in 217 organ(s), highest expression level in left lobe of thyroid gland
ExpressionAtlasiO00327 baseline and differential
GenevisibleiO00327 HS

Family and domain databases

CDDicd00083 HLH, 1 hit
cd00130 PAS, 2 hits
Gene3Di4.10.280.10, 1 hit
InterProiView protein in InterPro
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
IPR001067 Nuc_translocat
IPR001610 PAC
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold
PfamiView protein in Pfam
PF00010 HLH, 1 hit
PF00989 PAS, 1 hit
PRINTSiPR00785 NCTRNSLOCATR
SMARTiView protein in SMART
SM00353 HLH, 1 hit
SM00086 PAC, 1 hit
SM00091 PAS, 2 hits
SUPFAMiSSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits
TIGRFAMsiTIGR00229 sensory_box, 1 hit
PROSITEiView protein in PROSITE
PS50888 BHLH, 1 hit
PS50112 PAS, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBMAL1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O00327
Secondary accession number(s): A2I2N6
, A8K645, B5ME11, B7WPG7, D3DQW6, O00313, O00314, O00315, O00316, O00317, Q4G136, Q8IUT4, Q99631, Q99649
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 15, 2003
Last modified: January 16, 2019
This is version 194 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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